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从一株鼠抗ＢＭＰ单克隆抗体杂交瘤中扩增出其可变区基因片段，并将其分别克隆入ｐＵＣ１８、１９载体，利用双脱氧链终止法进行序列测定和计算机分析后，应用一段人工合成的含１５个氨基酸的连接肽，将重链基因（ＶＨ）的Ｃ端和轻链基因（ＶＬ）的Ｎ端连接起来，构建成单链抗体（ｓｃＦｖ）。将其克隆入融合蛋白表达载体ｐＧＥＸ－４Ｔ－１，在大肠杆菌ＪＭ１０９中获得初步表达。
A variable region gene fragment was amplified from a murine anti-BMP monoclonal antibody hybridoma and cloned into pUC18 and 19 vector respectively. After sequencing by dideoxy chain termination and computer analysis, The synthetic 15 amino acid linker peptide was constructed by linking the C terminus of the heavy chain gene (VH) with the N terminus of the light chain gene (VL) to form a single chain antibody (scFv). Cloned into the fusion protein expression vector pGEX-4T-1, the expression was obtained in E. coli JM109.